Analytical Data
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Gene name
NUP37
- Application
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Alternative Names
NUP37；Nucleoporin Nup37
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NFH4
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Expression Region
1-326aa
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AA Sequence
MKQDASRNAA YTVDCEDYVH VVEFNPFENG DSGNLIAYGG NNYVVIGTCT FQEEEADVEG IQYKTLRTFH HGVRVDGIAW SPETRLDSLP PVIKFCTSAA DMKIRLFTSD LQDKNEYKVL EGHTDFINGL VFDPKEGQEI ASVSDDHTCR IWNLEGVQTA HFVLHSPGMS VCWHPEETFK LMVAEKNGTI RFYDLLAQQA ILSLESEQVP LMSAHWCLKN TFKVGAVAGN DWLIWDITRS SYPQNKRPVH MDRACLFRWS TISENLFATT GYPGKMASQF QIHHLGHPQP ILMGSVAVGS GLSWHRTLPL CVIGGDHKLL FWVTEV
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Molecular Weight
36.7kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NUP37 is a crucial component of the nuclear pore complex (NPC), which plays a significant role in nucleocytoplasmic transport, mediating the exchange of molecules between the nucleus and the cytoplasm. The study of NUP37 recombinant protein has gained attention due to its potential implications in various cellular processes, including gene expression regulation and signal transduction. Dysregulation of NUP37 has been linked to several diseases, including cancer, highlighting its importance in cellular health and disease mechanisms. Furthermore, the recombinant production of NUP37 allows for detailed biochemical and biophysical characterization, facilitating the understanding of its structural properties and interaction with other nuclear pore components. This information could pave the way for the development of therapeutic strategies targeting NPC-related disorders. Additionally, studying NUP37 in various model systems enhances our understanding of the evolutionary conservation of nucleocytoplasmic transport mechanisms across species. The recombinant protein serves as a valuable tool for elucidating the functional roles of NUP37 and its interactions, thereby contributing to a broader comprehension of the complex regulatory networks governing cellular homeostasis.
